Evidence of Coupling between the Motions of Water and Peptides
Artikel i vetenskaplig tidskrift, 2016

Studies of protein dynamics at low temperatures are generally performed on hydrated powders and not in biologically realistic solutions of water because of water crystallization. However, here we avoid the problem of crystallization by reducing the size of the biomolecules. We have studied oligomers of the amino acid L-lysine, fully dissolved in water, and our dielectric relaxation data show that the glass transition-related dynamics of the oligomers is determined by the water dynamics, in a way similar to that previously observed for solvated proteins. This implies that the crucial role of water for protein dynamics can be extended to other types of macromolecular systems, where water is also able to determine their conformational fluctuations. Using the energy landscape picture of macromolecules, the thermodynamic criterion for such solvent-slaved macromolecular motions may be that the macromolecules need the entropy contribution from the solvent to overcome the enthalpy barriers between different conformational substates.

WATER

V106

SUPERCOOLED

PROTEIN DYNAMICS

SOLVENT

HYDRATION WATER

P5129

Materials Science

BOVINE SERUM-ALBUMIN

Chemistry

Molecular & Chemical

Physics

CONFINED WATER

RELAXATION

Atomic

GLASS-TRANSITION

LYSINE

ATES OF AMERICA

Nanoscience & Nanotechnology

MYOGLOBIN

Physical

Multidisciplinary

Författare

S. Cerveny

CSIC-UPV - Centro de Fisica de Materiales (CFM)

Donostia International Physics Center

I. Combarro-Palacios

CSIC-UPV - Centro de Fisica de Materiales (CFM)

Jan Swenson

Chalmers, Fysik, Kondenserade materiens fysik

Journal of Physical Chemistry Letters

1948-7185 (eISSN)

Vol. 7 20 4093-4098

Drivkrafter

Hållbar utveckling

Styrkeområden

Materialvetenskap

Ämneskategorier

Den kondenserade materiens fysik

DOI

10.1021/acs.jpclett.6b01864

Mer information

Skapat

2017-10-07